Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 20090

Title: KAAAD, single alpha helix turn   PubMed: 20543141

Deposition date: 2009-08-12 Original release date: 2010-10-13

Authors: Hoang, Huy

Citation: Harrisona, Rosemary; Shepherda, Nicholas; Hoanga, Huy; Ruiz-Gomeza, Gloria; Hilla, Timothy; Drivera, Russell; Desaib, Vishal; Youngb, Paul; Abbenantea, Giovanni; Fairliea, David. "Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency"  Proc. Natl. Acad. Sci. U. S. A. 107, 11686-11691 (2010).

Assembly members:
single_turn_helix, polymer, 5 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
single_turn_helix: KAAAD

Data sets:
Data typeCount
1H chemical shifts29
coupling constants5

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1Amino Acid1


Entity 1, Amino Acid 5 residues - Formula weight is not available



sample_1: single turn helix 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.5; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1


X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

NMR spectrometers:

  • Bruker AMX 900 MHz